Q9CB92 (END3_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endonuclease III
EC=4.2.99.18

Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase

Gene names

Name:	nth
Ordered Locus Names:	ML2301

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Incises damaged DNA at cytosines, thymines and guanines. Acts on a damaged strand, 5' from the damaged site By similarity.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Cofactor	Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the DNA strand By similarity.
Sequence similarities	Belongs to the Nth/MutY family.
Sequence caution	The sequence CAC31817.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	base-excision repair Inferred from electronic annotation. Source: InterPro
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC endonuclease activity Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 245	245	Endonuclease III		PRO_0000102218
Sites
	Metal binding	198	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	205	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	208	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	214	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CB92 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 1BF86C45306395D2	FASTA	245	27,194
	10 20 30 40 50 60 MARRWSGETR LGLVRRARRM NRALAQAFPH VYCELDFTSP LELTVATILS AQSTDKRVNL 70 80 90 100 110 120 TTPAVFARYR SALDYMQADR AELENFIRPT GFFRNKAASL IRLGQALVER FDGEVPSTMV 130 140 150 160 170 180 DLFTLPGVGR KTANVILGNA FGIPGITVDT HFGRLVRRWR WTAEEDPVKV EHAVGELIER 190 200 210 220 230 240 DQWTLLSHRV IFHGRRVCHA RKPACGVCVL AKDCPSFGLG PTEPLLAAPL VQGPEAGHLL ALAGL

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL583925 Genomic DNA. Translation: CAC31817.1. Different initiation.
PIR	A87197.
RefSeq	NP_302496.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q9CB92.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028867; EBMYCP00000028473; EBMYCG00000028862.
GeneID	908145.
GenomeReviews	Gene locus ML2301 in contig AL450380_GR.
KEGG	mle:ML2301.
NMPDR	fig|272631.1.peg.1368.
PATRIC	18058989. VBIMycLep78757_4411.
Organism-specific databases
Leproma	ML2301.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016637.
HOGENOM	HBG464473.
ProtClustDB	CLSK2460609.
Enzyme and pathway databases
BioCyc	MLEP272631:ML2301-MONOMER.
Family and domain databases
InterPro	IPR011257. DNA_glycosylase. IPR004036. Endonuclease-III_CS2. IPR005759. Endonuclease-III_Nth. IPR004035. Endouclease-III_FeS-bd_BS. IPR003651. Endouclease3_FeS-loop_motif. IPR003265. HhH-GPD_domain. IPR023170. HTH_base_excis_C. [Graphical view]
Gene3D	G3DSA:1.10.340.30. DNA_glycosylase. 1 hit. G3DSA:1.10.1670.10. HTH_base_excis_C. 1 hit.
KO	K10773.
Pfam	PF10576. EndIII_4Fe-2S. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
TIGRFAMs	TIGR01083. Nth. 1 hit.
PROSITE	PS00764. ENDONUCLEASE_III_1. 1 hit. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END3_MYCLE

Accession

Primary (citable) accession number: Q9CB92

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program